5 years ago

Biocatalytic Friedel–Crafts Acylation and Fries Reaction

Biocatalytic Friedel–Crafts Acylation and Fries Reaction
Tea Pavkov-Keller, Nina Richter, Wolfgang Kroutil, Karl Gruber, Nina G. Schmidt, Birgit Wiltschi
The Friedel–Crafts acylation is commonly used for the synthesis of aryl ketones, and a biocatalytic version, which may benefit from the chemo- and regioselectivity of enzymes, has not yet been introduced. Described here is a bacterial acyltransferase which can catalyze Friedel–Crafts C-acylation of phenolic substrates in buffer without the need of CoA-activated reagents. Conversions reach up to >99 %, and various C- or O-acyl donors, such as DAPG or isopropenyl acetate, are accepted by this enzyme. Furthermore the enzyme enables a Fries-like rearrangement reaction of resorcinol derivatives. These findings open an avenue for the development of alternative and selective C−C bond formation methods. Order up on Fries: The biocatalytic acylation of resorcinol substrates, catalyzed by an acyltransferase, leads to C-acylated products. The Friedel–Crafts bio-C-acylation allows use of simple activated esters, such as isopropenyl acetate, as an acyl source. Additionally the enzyme enables a Fries-like rearrangement reaction.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201703270

You might also like
Discover & Discuss Important Research

Keeping up-to-date with research can feel impossible, with papers being published faster than you'll ever be able to read them. That's where Researcher comes in: we're simplifying discovery and making important discussions happen. With over 19,000 sources, including peer-reviewed journals, preprints, blogs, universities, podcasts and Live events across 10 research areas, you'll never miss what's important to you. It's like social media, but better. Oh, and we should mention - it's free.

  • Download from Google Play
  • Download from App Store
  • Download from AppInChina

Researcher displays publicly available abstracts and doesn’t host any full article content. If the content is open access, we will direct clicks from the abstracts to the publisher website and display the PDF copy on our platform. Clicks to view the full text will be directed to the publisher website, where only users with subscriptions or access through their institution are able to view the full article.